We have recently shown that high resolution 1H NMR can in principle be used to determine three-dimensional conformations of small proteins in solution. This expanded capability requires the use of two-dimensional NMR methods such as 2D J-resolved spectroscopy, 2D correlated spectroscopy and 2D cross relaxation spectroscopy, as well as data analysis treatments based on a distance-geometry algorithm. Implementation, improvement and further evaluation of these methods is proposed. Because the lack of conformational information at the molecular level for membrane-sound proteins currently greatly restricts our understanding of membrane function, it is proposed that the use of the new NMR methodology for studies of the conformation, location, orientation and lipid-interactions of such proteins and polypeptides is a particularly suitable application. Although there are a large number of proteins and polypeptides of this type which are of potential interest, it is proposed to initiate work with specific projects for investigation of glycophorin A and polymyxin.